Interaction of vanadate with uridine and adenosine monophosphate.  Formation of ADP and ATP analogs

Tracey, Alan S.; Gresser, Michael J.; Liu, Susana

doi:10.1021/ja00225a044

Cited by 58 publications

(42 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…From the Y-intercept, a value of (2.1 2 0.3) x l o i 0 M -~ was calculated for K,,. This value is very close to those previously reported for the formation of the vanadate tetramer at this pH (17).…”

Section: Glycylhistidinesupporting

confidence: 92%

See 1 more Smart Citation

Condensation reactions between vanadate and small functionalized peptides in aqueous solution

Tracey¹,

Jaswal²,

Nxumalo³

et al. 1995

Can. J. Chem.

Self Cite

View full text Add to dashboard Cite

Abstract:The role that histidyl, seryl, tyrosyl, and other side chains of small peptides play in the formation of vanadate complexes has been investigated using 'H, I3c, and "V nuclear magnetic resonance spectroscopy. Formation constants of product complexes in aqueous solution have been determined and the influence of pH on the equilibria established. The results revealed that, in histidine-containing compounds, the protonation state of the imidazole ring of the free ligand strongly influences product formation. The results unequivocally showed that no vanadium-to-imidazole bond was formed for any of the histidine-containing complexes studied. However, imidazole and other aromatic side-chain residues have an effect on product stability via their influence on the protonation state (pK,) of the products. Aliphatic side-chains, such as those in asparagine or glutamate, do not appear to play a significant role in the formation of products. This is not true, however, of serine or threonine where the side-chains readily generate vanadium-oxygen bonds.

show abstract

Section: Glycylhistidinesupporting

confidence: 92%

“…Experimental rcsults rrom a detailed study of the reaction or this dipeptide with vanadatc have been rcported (17). These results were intcrprcted to mean that in addition to the expccted mononuclear ~nonoligand product, VP, an additional binuclear bisligand product (V2P) was rormcd.…”

Section: Plienylglutamatementioning

confidence: 99%

Condensation reactions between vanadate and small functionalized peptides in aqueous solution

Tracey¹,

Jaswal²,

Nxumalo³

et al. 1995

Can. J. Chem.

Self Cite

View full text Add to dashboard Cite

show abstract

“…Preparation of Vanadate and Pervanadate-Vanadate stock solution was prepared by dissolving vanadium(V) oxide in 2.1 molar equivalents of 1 N NaOH, stirring the solution until the yellow color had essentially disappeared (2-3 days), and then diluting with water to a final concentration of 100 mM (30). Pervanadate stock solution (1 mM) was prepared by adding 10 l of 100 mM vanadate and 50 l of 100 mM hydrogen peroxide (diluted from a 30% stock in 20 mM HEPES, pH 7.3) to 940 l of H 2 O.…”

Section: Methodsmentioning

confidence: 99%

Mechanism of Inhibition of Protein-tyrosine Phosphatases by Vanadate and Pervanadate

Huyer

Liu²,

Kelly

et al. 1997

Journal of Biological Chemistry

Self Cite

776

592

View full text Add to dashboard Cite

Vanadate and pervanadate (the complexes of vanadate with hydrogen peroxide) are two commonly used general protein-tyrosine phosphatase (PTP) inhibitors. These compounds also have insulin-mimetic properties, an observation that has generated a great deal of interest and study. Since a careful kinetic study of the two inhibitors has been lacking, we sought to analyze their mechanisms of inhibition. Our results show that vanadate is a competitive inhibitor for the protein-tyrosine phosphatase PTP1B, with a K i of 0.38 ؎ 0.02 M. EDTA, which is known to chelate vanadate, causes an immediate and complete reversal of the inhibition due to vanadate when added to an enzyme assay. Pervanadate, by contrast, inhibits by irreversibly oxidizing the catalytic cysteine of PTP1B, as determined by mass spectrometry. Reducing agents such as dithiothreitol that are used in PTP assays to keep the catalytic cysteine reduced and active were found to convert pervanadate rapidly to vanadate. Under certain conditions, slow time-dependent inactivation by vanadate was observed; since catalase blocked this inactivation, it was ascribed to in situ generation of hydrogen peroxide and subsequent formation of pervanadate. Implications for the use of these compounds as inhibitors and rationalization for some of their in vivo effects are considered.Protein-tyrosine phosphorylation plays a central role in regulating a variety of fundamental cellular processes (1-3). The tyrosyl phosphorylation state of a protein in the cell reflects the balance between the competing activities of the protein-tyrosine kinases and the protein tyrosine phosphatases (PTPs).

show abstract

“…The interactions of vanadate with nucleosides (4,(16)(17)(18)(19)(20) and P-methylriboside (5) have been studied by a number of workers. These studies have clearly shown that, under conditions of a few millimolar concentrations of vanadate with equivalent amounts of ligand at neutral pH, the major product of the reaction is a binuclear bisligand product.…”

Section: Uridine 56-dihydrouridine and Methyl P-dribofuranoside Plmentioning

confidence: 99%

Influence of vanadium(V) complexes on the catalytic activity of ribonuclease A. The role of vanadate complexes as transition state analogues to reactions at phosphate

Leon-Lai¹,

Gresser²,

Tracey³

1996

Can. J. Chem.

Self Cite

View full text Add to dashboard Cite

Abstract:The interactions of vanadate and its complexes of uridine, 5,6-dihydrouridine, and methyl P-D-ribofuranoside with bovine pancreatic ribonuclease A (RNase A) (EC 3.1.27.5) were studied by 5 1~ NMR spectroscopy and enzyme kinetics. From kinetic studies, it was found that neither inorganic vanadate nor the methyl P-D-ribofuranoside-vanadate complex significantly inhibited the RNase A catalyzed hydrolysis of uridine 2',3'-cyclic monophosphate. The NMR binding studies were in full agreement with the kinetics studies and showed that neither inorganic vanadate nor the methyl P-D-ribofuranoside-vanadate complex was bound tightly by the enzyme. Approximate binding constants were (5.0 + 1.0) x M and (3.0 + 0.6) x M for the uridine-and 5.6-dihydrouridine-vanadate complexes, respectively. An induced-fit mechanism is suggested, in which the pyrimidine subsite of the active site of RNase A must be fully occupied for the enzyme to be able to tightly bind the transition state or transition state analog. Calculation of the binding energies of vanadate complexes in ribonuclease, phosphoglycerate mutase, and phosphoglucomutase revealed an excess of binding energy over the analogous phosphate derivative of about 25 kJ/mol for all enzymes, even though the binding constants themselves varied by about six orders of magnitude. This energy represents about 40% of that expected to be available for a trigonal-bipyramidal transition state and requires a reassessment of the role of vanadate as a transition state analogue for phosphate transfer.Key words: vanadate, ribonuclease, transition state, binding constants, phosphate analogues, kinetics.Resum6 : Faisant appel a la spectrscopie RMN du 5 1~ et de la cinCtique des enzymes, on a CtudiC les interactions entre le vanadate et ses complexes de I'uridine, de la 5,6-dihydrouridine et du P-D-ribofuranoside de mCthyle avec la ribunuclease A du pancrCas de boeuf (RNase A) (EC 3.1.27.5). Sur la base des Ctudes cinCtiques, on a trouvC que, vis-a-vis de I'hydrolyse du monophosphate 2',3'-cyclique de I'uridine de la RNase A, ni le vanadate inorganique ni le complexe du P-D-ribofuranoside de mCthyle-vanadate n'inhibent cette rCaction d'une f a~o n significative. Les Ctudes par RMN ont montrt qu'il ne se produit aucune fixation entre ces matCriaux et elles Ctaient en parfait accord avec les ttudes cinCtiques; elles montrent aussi que ni le vanadate inorganique ni le complexe du P-D-ribofuranoside de mCthyle-vanadate ne se complexent fortement avec I'enzyme. Les constantes apparentes de fixation ont respectivement de (5,O + 1.0) x M et (3,O + 0.6) x M pour les complexes de I'uridine et du 5,6-dihydrouridine avec le vanadate. On propose un mCcanisme induit d'ajustement dans lequel il est important que tout le sous site de la pyrimidine du site actif de la RNase A soit occupC pour que I'enzyme soit capable de bien fixer 1'Ctat de transition ou son analogue. Des calculs d'Cnergie de fixation des complexes du vanadate dans la ribonucltase, la phosphoglycCratemutase ou la phosphoglucomutase ont rCvC...

show abstract

Interaction of vanadate with uridine and adenosine monophosphate. Formation of ADP and ATP analogs

Cited by 58 publications

References 10 publications

Condensation reactions between vanadate and small functionalized peptides in aqueous solution

Condensation reactions between vanadate and small functionalized peptides in aqueous solution

Mechanism of Inhibition of Protein-tyrosine Phosphatases by Vanadate and Pervanadate

Influence of vanadium(V) complexes on the catalytic activity of ribonuclease A. The role of vanadate complexes as transition state analogues to reactions at phosphate

Contact Info

Product

Resources

About